BMRB Entry 16183
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16183
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Title: Tammar Wallaby Prion Protein (121-230) PubMed: 19393664
Deposition date: 2009-02-24 Original release date: 2009-05-20
Authors: Christen, Barbara; Hornemann, Simone; Damberger, Fred; Wuthrich, Kurt
Citation: Christen, Barbara; Hornemann, Simone; Damberger, Fred; Wuthrich, Kurt. "Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects." J. Mol. Biol. 389, 833-845 (2009).
Assembly members:
wpp_121-230, polymer, 112 residues, 13167.715 Da.
Natural source: Common Name: tammar wallaby Taxonomy ID: 9315 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Macropus Eugenii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
wpp_121-230: GSVVGGLGGYMLGSAMSRPV
MHFGNEYEDRYYRENQYRYP
NQVMYRPIDQYGSQNSFVHD
CVNITVKQHTTTTTTKGENF
TETDIKIMERVVEQMCITQY
QNEYQAAQRYYN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 473 |
| 15N chemical shifts | 132 |
| 1H chemical shifts | 782 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | wpp_121-230 | 1 |
Entities:
Entity 1, wpp_121-230 112 residues - 13167.715 Da.
| 1 | GLY | SER | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | ||||
| 2 | MET | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | VAL | ||||
| 3 | MET | HIS | PHE | GLY | ASN | GLU | TYR | GLU | ASP | ARG | ||||
| 4 | TYR | TYR | ARG | GLU | ASN | GLN | TYR | ARG | TYR | PRO | ||||
| 5 | ASN | GLN | VAL | MET | TYR | ARG | PRO | ILE | ASP | GLN | ||||
| 6 | TYR | GLY | SER | GLN | ASN | SER | PHE | VAL | HIS | ASP | ||||
| 7 | CYS | VAL | ASN | ILE | THR | VAL | LYS | GLN | HIS | THR | ||||
| 8 | THR | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | ||||
| 9 | THR | GLU | THR | ASP | ILE | LYS | ILE | MET | GLU | ARG | ||||
| 10 | VAL | VAL | GLU | GLN | MET | CYS | ILE | THR | GLN | TYR | ||||
| 11 | GLN | ASN | GLU | TYR | GLN | ALA | ALA | GLN | ARG | TYR | ||||
| 12 | TYR | ASN |
Samples:
sample_1: sodium acetate, [U-100% 2H], 10 mM; entity, [U-99% 13C; U-99% 15N], 1.5 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)C(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - data analysis
ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking
DYANA v1.0.3, Guntert, Mumenthaler and Wuthrich - structure solution
OPALP, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
Molmol, Koradi, Billeter and Wuthrich - data analysis
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts